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LongText Report for: 7a43-pdb

Name Class
7a43-pdb
HEADER    HYDROLASE                               19-AUG-20   7A43              
TITLE     FLUOROACETATE DEHALOGENASE MEASURED BY SERIAL FEMTOSECOND             
TITLE    2 CRYSTALLOGRAPHY                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLUOROACETATE DEHALOGENASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.8.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;                     
SOURCE   3 ORGANISM_TAXID: 1076;                                                
SOURCE   4 GENE: RPA1163;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DEHALOGENASE, SERIAL FEMTOSECOND CRYSTALLOGRAPHY, HYDROLASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.MEHRABI,E.C.SCHULZ,R.BUECKER                                        
REVDAT   1   07-APR-21 7A43    0                                                
JRNL        AUTH   P.MEHRABI,R.BUCKER,G.BOURENKOV,H.M.GINN,D.VON STETTEN,       
JRNL        AUTH 2 H.M.MULLER-WERKMEISTER,A.KUO,T.MORIZUMI,B.T.EGER,W.L.OU,     
JRNL        AUTH 3 S.OGHBAEY,A.SARRACINI,J.E.BESAW,O.PARE-LABROSSE,S.MEIER,     
JRNL        AUTH 4 H.SCHIKORA,F.TELLKAMP,A.MARX,D.A.SHERRELL,D.AXFORD,R.L.OWEN, 
JRNL        AUTH 5 O.P.ERNST,E.F.PAI,E.C.SCHULZ,R.J.D.MILLER                    
JRNL        TITL   SERIAL FEMTOSECOND AND SERIAL SYNCHROTRON CRYSTALLOGRAPHY    
JRNL        TITL 2 CAN YIELD DATA OF EQUIVALENT QUALITY: A SYSTEMATIC           
JRNL        TITL 3 COMPARISON.                                                  
JRNL        REF    SCI ADV                       V.   7       2021              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   33731353                                                     
JRNL        DOI    10.1126/SCIADV.ABF1380                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18_3855                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53205                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.450                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1838                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.0800 -  4.1100    1.00     4155   150  0.1526 0.1660        
REMARK   3     2  4.1100 -  3.2700    1.00     4091   148  0.1420 0.1722        
REMARK   3     3  3.2600 -  2.8500    1.00     4071   147  0.1622 0.1941        
REMARK   3     4  2.8500 -  2.5900    0.99     4049   146  0.1683 0.1906        
REMARK   3     5  2.5900 -  2.4100    0.99     4058   141  0.1623 0.2097        
REMARK   3     6  2.4100 -  2.2600    0.99     4042   139  0.1560 0.1924        
REMARK   3     7  2.2600 -  2.1500    0.99     4005   141  0.1558 0.1973        
REMARK   3     8  2.1500 -  2.0600    0.98     3987   136  0.1672 0.2172        
REMARK   3     9  2.0600 -  1.9800    0.97     3917   142  0.1713 0.2109        
REMARK   3    10  1.9800 -  1.9100    0.96     3867   146  0.1748 0.2633        
REMARK   3    11  1.9100 -  1.8500    0.94     3844   143  0.1833 0.2630        
REMARK   3    12  1.8500 -  1.8000    0.91     3693   129  0.2079 0.2428        
REMARK   3    13  1.8000 -  1.7500    0.89     3588   130  0.2250 0.2678        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.177            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.231           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           4902                                  
REMARK   3   ANGLE     :  1.252           6685                                  
REMARK   3   CHIRALITY :  0.067            685                                  
REMARK   3   PLANARITY :  0.009            881                                  
REMARK   3   DIHEDRAL  : 36.454            665                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7A43 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292110817.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : BL3                                
REMARK 200  X-RAY GENERATOR MODEL          : SACLA BEAMLINE BL3                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.22                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MPCCD                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL                           
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54828                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 101.9                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 3.8800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3R3U                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20 % (W/V)) PEG3350, 200 MM CACL2,    
REMARK 280  AND 100 MM TRIS-HCL PH 8.5, BATCH MODE, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.95000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     SER A   304                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     ALA B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     GLY B   303                                                      
REMARK 465     SER B   304                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A   3    CG   OD1  OD2                                       
REMARK 470     ARG A 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 259    OG1  CG2                                            
REMARK 470     ARG B 296    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   556     O    HOH A   581              2.10            
REMARK 500   O    HOH A   627     O    HOH A   631              2.18            
REMARK 500   O    HOH A   556     O    HOH B   561              2.18            
REMARK 500   O    HOH A   580     O    HOH A   629              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  41       64.52   -103.13                                   
REMARK 500    ASP A 110     -128.84     60.32                                   
REMARK 500    SER A 123       56.06   -144.69                                   
REMARK 500    ILE A 153       50.84   -115.66                                   
REMARK 500    ASP A 173       72.52   -157.42                                   
REMARK 500    TYR A 224      -97.90   -121.84                                   
REMARK 500    PRO B  41       66.76   -105.08                                   
REMARK 500    ASP B 110     -129.87     57.46                                   
REMARK 500    SER B 123       58.33   -141.52                                   
REMARK 500    ILE B 153       51.05   -112.67                                   
REMARK 500    ASP B 173       74.17   -162.34                                   
REMARK 500    TYR B 224      -97.38   -119.95                                   
REMARK 500    ALA B 286       59.78   -146.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401                  
DBREF  7A43 A    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
DBREF  7A43 B    1   302  UNP    Q6NAM1   DEHA_RHOPA       1    302             
SEQADV 7A43 GLY A   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 HIS A    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 GLY A  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 SER A  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 GLY B   -1  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 HIS B    0  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 GLY B  303  UNP  Q6NAM1              EXPRESSION TAG                 
SEQADV 7A43 SER B  304  UNP  Q6NAM1              EXPRESSION TAG                 
SEQRES   1 A  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 A  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 A  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 A  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 A  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 A  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 A  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 A  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 A  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 A  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 A  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 A  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 A  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 A  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 A  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 A  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 A  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 A  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 A  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 A  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 A  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 A  306  GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU          
SEQRES  23 A  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 A  306  PHE SER ALA ALA PRO GLY SER                                  
SEQRES   1 B  306  GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE          
SEQRES   2 B  306  GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE          
SEQRES   3 B  306  ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU          
SEQRES   4 B  306  HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL          
SEQRES   5 B  306  ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA          
SEQRES   6 B  306  ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER          
SEQRES   7 B  306  ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA          
SEQRES   8 B  306  LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL          
SEQRES   9 B  306  HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL          
SEQRES  10 B  306  SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER          
SEQRES  11 B  306  LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR          
SEQRES  12 B  306  TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR          
SEQRES  13 B  306  HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU          
SEQRES  14 B  306  ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA          
SEQRES  15 B  306  LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA          
SEQRES  16 B  306  PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE          
SEQRES  17 B  306  ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR          
SEQRES  18 B  306  ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE          
SEQRES  19 B  306  ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU          
SEQRES  20 B  306  ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA          
SEQRES  21 B  306  THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL          
SEQRES  22 B  306  GLN GLY ALA PRO ILE GLU SER GLY HIS PHE LEU PRO GLU          
SEQRES  23 B  306  GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE          
SEQRES  24 B  306  PHE SER ALA ALA PRO GLY SER                                  
HET     CL  A 401       1                                                       
HET     CL  B 401       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  HOH   *306(H2 O)                                                    
HELIX    1 AA1 THR A   43  HIS A   48  5                                   6    
HELIX    2 AA2 VAL A   50  GLU A   56  1                                   7    
HELIX    3 AA3 HIS A   80  TYR A   83  5                                   4    
HELIX    4 AA4 THR A   84  LEU A   99  1                                  16    
HELIX    5 AA5 ASP A  110  SER A  123  1                                  14    
HELIX    6 AA6 PRO A  137  ARG A  144  1                                   8    
HELIX    7 AA7 ASN A  146  ILE A  153  1                                   8    
HELIX    8 AA8 ILE A  153  LEU A  159  1                                   7    
HELIX    9 AA9 PRO A  164  GLY A  171  1                                   8    
HELIX   10 AB1 ASP A  173  TRP A  185  1                                  13    
HELIX   11 AB2 ASP A  195  ALA A  207  1                                  13    
HELIX   12 AB3 ASP A  208  TYR A  224  1                                  17    
HELIX   13 AB4 TYR A  224  GLY A  237  1                                  14    
HELIX   14 AB5 THR A  259  ALA A  268  1                                  10    
HELIX   15 AB6 PHE A  281  ALA A  286  1                                   6    
HELIX   16 AB7 ALA A  286  ALA A  300  1                                  15    
HELIX   17 AB8 THR B   43  HIS B   48  5                                   6    
HELIX   18 AB9 VAL B   50  ALA B   55  1                                   6    
HELIX   19 AC1 HIS B   80  TYR B   83  5                                   4    
HELIX   20 AC2 THR B   84  LEU B   99  1                                  16    
HELIX   21 AC3 ASP B  110  SER B  123  1                                  14    
HELIX   22 AC4 PRO B  137  ARG B  144  1                                   8    
HELIX   23 AC5 ASN B  146  ILE B  153  1                                   8    
HELIX   24 AC6 TYR B  154  LEU B  159  1                                   6    
HELIX   25 AC7 PRO B  164  GLY B  171  1                                   8    
HELIX   26 AC8 ASP B  173  TRP B  185  1                                  13    
HELIX   27 AC9 ASP B  195  ASP B  208  1                                  14    
HELIX   28 AD1 ASP B  208  TYR B  224  1                                  17    
HELIX   29 AD2 TYR B  224  GLY B  237  1                                  14    
HELIX   30 AD3 ILE B  253  ALA B  258  1                                   6    
HELIX   31 AD4 THR B  259  LYS B  266  1                                   8    
HELIX   32 AD5 PHE B  281  ALA B  286  1                                   6    
HELIX   33 AD6 ALA B  286  SER B  299  1                                  14    
SHEET    1 AA1 8 GLY A  12  ILE A  16  0                                        
SHEET    2 AA1 8 ILE A  23  GLY A  29 -1  O  ILE A  23   N  ILE A  16           
SHEET    3 AA1 8 LYS A  59  ALA A  63 -1  O  VAL A  62   N  ARG A  26           
SHEET    4 AA1 8 PRO A  33  LEU A  37  1  N  LEU A  34   O  ILE A  61           
SHEET    5 AA1 8 PHE A 104  HIS A 109  1  O  ALA A 105   N  LEU A  35           
SHEET    6 AA1 8 LEU A 127  LEU A 133  1  O  ALA A 131   N  LEU A 106           
SHEET    7 AA1 8 MET A 244  GLY A 249  1  O  LEU A 247   N  VAL A 132           
SHEET    8 AA1 8 VAL A 271  ILE A 276  1  O  GLN A 272   N  ALA A 246           
SHEET    1 AA2 8 GLY B  12  ILE B  16  0                                        
SHEET    2 AA2 8 ILE B  23  GLY B  28 -1  O  VAL B  27   N  GLY B  12           
SHEET    3 AA2 8 LYS B  59  ALA B  63 -1  O  VAL B  62   N  ARG B  26           
SHEET    4 AA2 8 PRO B  33  LEU B  37  1  N  LEU B  34   O  ILE B  61           
SHEET    5 AA2 8 PHE B 104  HIS B 109  1  O  ALA B 105   N  LEU B  35           
SHEET    6 AA2 8 LEU B 127  LEU B 133  1  O  ALA B 131   N  LEU B 106           
SHEET    7 AA2 8 MET B 244  GLY B 249  1  O  LEU B 245   N  VAL B 132           
SHEET    8 AA2 8 VAL B 271  ILE B 276  1  O  ILE B 276   N  TRP B 248           
CISPEP   1 PHE A   40    PRO A   41          0        -1.77                     
CISPEP   2 ALA A  163    PRO A  164          0         2.37                     
CISPEP   3 PHE B   40    PRO B   41          0        -1.68                     
CISPEP   4 ALA B  163    PRO B  164          0         0.16                     
SITE     1 AC1  4 ASP A 110  ARG A 114  HOH A 513  HOH A 642                    
SITE     1 AC2  3 ASP B 110  ARG B 114  HOH B 501                               
CRYST1   41.900   79.900   84.800  90.00 103.40  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023866  0.000000  0.005686        0.00000                         
SCALE2      0.000000  0.012516  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012122        0.00000                         
TER    2395      ALA A 300                                                      
TER    4745      SER B 299                                                      
MASTER      282    0    2   33   16    0    2    6 4998    2    0   48          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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